Peptidomics [[electronic resource] ] : methods and applications / / edited by Mikhail Soloviev, Chris Shaw, Per Andrén |
Pubbl/distr/stampa | Hoboken, N.J., : Wiley-Interscience, c2008 |
Descrizione fisica | 1 online resource (432 p.) |
Disciplina | 612/.015756 |
Altri autori (Persone) |
SolovievMikhail <1965->
ShawChris <1954-> AndrénPer |
Soggetto topico |
Peptides
Proteomics |
ISBN |
1-281-22166-X
9786611221669 0-470-19650-5 0-470-19649-1 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
PEPTIDOMICS; CONTENTS; Preface; Contributors; PART I STUDIES OF NATURALLY OCCURRING PEPTIDES; 1 Analysis of the Peptidomes of Amphibian Skin Granular Gland Secretions-An Integrated Functional Genomic Strategy; 1.1 Introduction; 1.2 Historical Perspective; 1.3 Contemporary Methods of Sample Acquisition; 1.4 The Integrated Functional Genomic Strategy; 1.5 How then can All Three Approaches be Integrated?; 1.6 Limitations of Each Approach; 1.7 Closing Thoughts
2 A Short History of Insect (Neuro)Peptidomics-A Personal Story of the Birth and Youth of an Excellent Model For Studying Peptidome Biology2.1 Introduction; 2.2 History; 2.3 Present (and Future): Novel Technologies, New Data. . .; 2.3.1 MALDI and (Nano)ESI TOFs and QTOFs; 2.3.2 Peptide Displays; 2.3.3 Ion Traps and FT-ICRs: Greater Variety of Instruments, Greater Variety of Sequences. . .; 2.3.4 Orbitrap; 2.3.5 FT-ICRs; 2.3.6 Combining Peptide Chemical Analysis with Histological Localization: Peptidome Mass Spectrometry Imaging; 2.4 Concluding Remarks 3 Peptidomics of Short Linear Cytolytic Peptides from Spider Venom3.1 Introduction; 3.2 Peptidomics: Identifying and Sequencing Novel AMPs; 3.3 Genomics: Unraveling the Biosynthetic Pathway; 3.4 Venomics: AMPs in the Spider Venom; 3.4.1 Structural Features; 3.4.2 Functional Features; 3.4.3 Venomic Significance; 4 Molecular Cloning Approaches to Peptidomics: The Identification of Novel cDNAs Encoding Neurotoxin-like Peptide Pools; 4.1 Introduction; 4.2 Spider Toxins-Combinatorial Peptide Libraries; 4.3 EST Cloning Approach to Cloning Peptide Families 4.4 PCR-Based Amplification and Cloning Approaches4.5 The Design and Use of Hybrid Primers for the Amplification of cDNAs Coding for Large Toxin-like Peptide Pools; 4.5.1 Multiple Alignment of the Existing Toxins and Toxin-like Sequences; 4.5.2 The Design of Hybrid Partially Degenerate Primers; 4.5.2.1 The Design of the 3 ́ Region; 4.5.2.2 The Design of the 5 ́ Region and the Middle Part of the Primers; 4.5.2.3 The Overall Length and Degeneracy; 4.5.2.4 Annealing Temperature Matching; 4.5.3 Optimization of the Amplification Conditions; 4.5.4 Other Experimental Details 4.5.5 High Throughout Amplification and Cloning4.5.6 Sequences Identification and Analysis; 4.6 Polypeptide Toxins-Novel Applications in Drug and Pesticide Development; 4.6.1 Analgesic Drugs; 4.6.2 Insecticides; 4.7 Concluding Remarks; 4.7.1 RACE-PCR Issues; 4.7.2 Sequence Quality Issues; 4.7.3 Conclusion; 5 Wheat Antimicrobial Peptides; 5.1 Introduction; 5.2 Materials and Methods; 5.2.1 Isolation of AMPs; 5.2.2 Reduction and Alkylation of Peptides [35]; 5.2.3 MALDI-TOF MS; 5.2.4 High-Resolution Two-Dimensional Gel Electrophoresis; 5.3 Isolation of AMPs from T. kiharae Seeds 5.4 Sequence Determination of AMPs from T. kiharae Seeds |
Record Nr. | UNINA-9910145556503321 |
Hoboken, N.J., : Wiley-Interscience, c2008 | ||
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Lo trovi qui: Univ. Federico II | ||
|
Peptidomics [[electronic resource] ] : methods and applications / / edited by Mikhail Soloviev, Chris Shaw, Per Andrén |
Pubbl/distr/stampa | Hoboken, N.J., : Wiley-Interscience, c2008 |
Descrizione fisica | 1 online resource (432 p.) |
Disciplina | 612/.015756 |
Altri autori (Persone) |
SolovievMikhail <1965->
ShawChris <1954-> AndrénPer |
Soggetto topico |
Peptides
Proteomics |
ISBN |
1-281-22166-X
9786611221669 0-470-19650-5 0-470-19649-1 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
PEPTIDOMICS; CONTENTS; Preface; Contributors; PART I STUDIES OF NATURALLY OCCURRING PEPTIDES; 1 Analysis of the Peptidomes of Amphibian Skin Granular Gland Secretions-An Integrated Functional Genomic Strategy; 1.1 Introduction; 1.2 Historical Perspective; 1.3 Contemporary Methods of Sample Acquisition; 1.4 The Integrated Functional Genomic Strategy; 1.5 How then can All Three Approaches be Integrated?; 1.6 Limitations of Each Approach; 1.7 Closing Thoughts
2 A Short History of Insect (Neuro)Peptidomics-A Personal Story of the Birth and Youth of an Excellent Model For Studying Peptidome Biology2.1 Introduction; 2.2 History; 2.3 Present (and Future): Novel Technologies, New Data. . .; 2.3.1 MALDI and (Nano)ESI TOFs and QTOFs; 2.3.2 Peptide Displays; 2.3.3 Ion Traps and FT-ICRs: Greater Variety of Instruments, Greater Variety of Sequences. . .; 2.3.4 Orbitrap; 2.3.5 FT-ICRs; 2.3.6 Combining Peptide Chemical Analysis with Histological Localization: Peptidome Mass Spectrometry Imaging; 2.4 Concluding Remarks 3 Peptidomics of Short Linear Cytolytic Peptides from Spider Venom3.1 Introduction; 3.2 Peptidomics: Identifying and Sequencing Novel AMPs; 3.3 Genomics: Unraveling the Biosynthetic Pathway; 3.4 Venomics: AMPs in the Spider Venom; 3.4.1 Structural Features; 3.4.2 Functional Features; 3.4.3 Venomic Significance; 4 Molecular Cloning Approaches to Peptidomics: The Identification of Novel cDNAs Encoding Neurotoxin-like Peptide Pools; 4.1 Introduction; 4.2 Spider Toxins-Combinatorial Peptide Libraries; 4.3 EST Cloning Approach to Cloning Peptide Families 4.4 PCR-Based Amplification and Cloning Approaches4.5 The Design and Use of Hybrid Primers for the Amplification of cDNAs Coding for Large Toxin-like Peptide Pools; 4.5.1 Multiple Alignment of the Existing Toxins and Toxin-like Sequences; 4.5.2 The Design of Hybrid Partially Degenerate Primers; 4.5.2.1 The Design of the 3 ́ Region; 4.5.2.2 The Design of the 5 ́ Region and the Middle Part of the Primers; 4.5.2.3 The Overall Length and Degeneracy; 4.5.2.4 Annealing Temperature Matching; 4.5.3 Optimization of the Amplification Conditions; 4.5.4 Other Experimental Details 4.5.5 High Throughout Amplification and Cloning4.5.6 Sequences Identification and Analysis; 4.6 Polypeptide Toxins-Novel Applications in Drug and Pesticide Development; 4.6.1 Analgesic Drugs; 4.6.2 Insecticides; 4.7 Concluding Remarks; 4.7.1 RACE-PCR Issues; 4.7.2 Sequence Quality Issues; 4.7.3 Conclusion; 5 Wheat Antimicrobial Peptides; 5.1 Introduction; 5.2 Materials and Methods; 5.2.1 Isolation of AMPs; 5.2.2 Reduction and Alkylation of Peptides [35]; 5.2.3 MALDI-TOF MS; 5.2.4 High-Resolution Two-Dimensional Gel Electrophoresis; 5.3 Isolation of AMPs from T. kiharae Seeds 5.4 Sequence Determination of AMPs from T. kiharae Seeds |
Record Nr. | UNINA-9910814904803321 |
Hoboken, N.J., : Wiley-Interscience, c2008 | ||
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Lo trovi qui: Univ. Federico II | ||
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Peptidomics |
Pubbl/distr/stampa | Warsaw, Poland : , : De Gruyter Open |
Descrizione fisica | 1 online resource |
Soggetto topico | Peptides |
Soggetto genere / forma |
Periodicals.
Periodical |
ISSN | 2084-7203 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Periodico |
Lingua di pubblicazione | eng |
Record Nr. | UNINA-9910131777103321 |
Warsaw, Poland : , : De Gruyter Open | ||
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Lo trovi qui: Univ. Federico II | ||
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Plant cyclotides / / volume editor, David J. Craik, Institute for Molecular Bioscience, the University of Queensland, Brisbane, QLD, Australia |
Edizione | [First edition.] |
Pubbl/distr/stampa | Amsterdam : , : Elsevier, , 2015 |
Descrizione fisica | 1 online resource (404 p.) |
Collana | Advances in botanical research |
Soggetto topico |
Botany - Research
Plant molecular biology Plant proteomics Peptides Botanical chemistry |
Soggetto genere / forma | Electronic books. |
ISBN |
0-12-800030-9
0-12-800797-4 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Front Cover; ADVANCES IN BOTANICAL RESEARCH; Plant Cyclotides; Copyright; Contents; CONTRIBUTORS; PREFACE; One - Overview on the Discovery and Applications of Cyclotides; 1. INTRODUCTION; ACKNOWLEDGMENTS; REFERENCES; Two - Cyclotides in the Violaceae; 1. THE DISCOVERY OF CYCLOTIDES IN VIOLACEAE; 2. UNLOCKING THE CYCLOTIDE LIBRARY; 3. THE VIOLACEAE; 4. VIOLACEAE-THE PHARMACOPOEIA; 5. GROWING NEEDS AND SOURCES OF CYCLOTIDES; 6. COMPLETING THE CIRCLE; ACKNOWLEDGMENTS; REFERENCES; Three - Cyclotides in the Rubiaceae; 1. INTRODUCTION; 2. DISCOVERY OF CYCLOTIDES
2.1 Cyclotide Analytical Screening Workflow2.2 Cyclotides Sequence Analysis Using Transcriptomics and Peptidomics; 3. DISTRIBUTION OF CYCLOTIDES IN RUBIACEAE; 3.1 Rubiaceae-An Overview; 3.2 Morphology and Taxonomy of Rubiaceae; 3.3 Distribution of Cyclotides within Rubiaceae; 3.4 Cyclotide Precursors of Rubiaceae Plants; 3.5 Cyclotide Sequence Variations within Rubiaceae; 3.6 Distribution of Cyclotides in Other Gentianales; 4. EVOLUTION OF CYCLOTIDES; 5. BIOACTIVITIES OF RUBIACEAE CYCLOTIDES; 6. CONCLUSION AND OUTLOOK; ACKNOWLEDGMENTS; REFERENCES; Four - Cyclotides from Chinese Plants 1. Introduction2. Chemical Detection Method for Cyclotides; 3. Distribution and Chemotaxonomy of Cyclotides in Chinese Plants; 4. Extraction, Isolation and Structural Elucidation of Cyclotides in Chinese Plants; 4.1 Extraction and Isolation of Cyclotides in Chinese Plants; 4.2 Tandem MS Sequencing of Cyclotides in Chinese Plants; 4.3 NMR Characterization of Cyclotides in Chinese Plants; 5. Biological Activity of Cyclotides in Chinese Plants; Acknowledgments; References; Five - Primary Structural Analysis of Cyclotides; 1. CYCLOTIDE DISCOVERY-UNTANGLING THE CYSTINE KNOT 2. TOOLS FOR PEPTIDE SEQUENCE ASSIGNMENT2.1 Gene Sequencing; 2.2 Genome Mining; 2.3 Next-Generation Sequencing; 2.4 Peptide Extraction and Purification; 2.5 Acid Hydrolysis and Amino Acid Analysis; 2.6 Edman Degradation; 2.7 Chemical and Enzymatic Digestion; 3. MASS SPECTROMETRY; 3.1 Ionization; 3.1.1 Electrospray Ionization; 3.1.2 Nanoelectrospray Ionization; 3.1.3 Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry; 3.2 Mass Analyzers; 3.2.1 Quadrupole Mass Analyzers; 3.2.2 TOF Mass Analyzers; 3.3 Peptide Sequencing; 4. APPLICATION OF MASS SPECTROMETRY TO CYCLOTIDE SEQUENCING 4.1 MS Analysis of Cyclotides4.2 Tandem Mass Spectrometric (MS/MS) Analysis of Cyclotides; 4.3 Application of "Omics" Technologies to Cyclotide Sequencing; 5. CHALLENGES AND COMPLEXITIES; 5.1 Co-eluting, Isobaric Peptides; 5.2 N/D Isoforms; 5.3 Unknown Genomes/Incomplete DBs; 6. FUTURE PROSPECTS; 6.1 Transcriptomics and Bioinformatics; 6.2 Automation and Robotics; 6.3 Advances in MS Hardware; 6.4 Advances in MS Software; 7. CONCLUDING REMARKS; REFERENCES; Six - Structural Studies of Cyclotides; 1. THE CYCLIC CYSTINE KNOT; 2. STRUCTURAL FEATURES OF CYCLOTIDES; 2.1 Structural Studies 2.2 Möbius, Bracelets, and Trypsin Inhibitors |
Record Nr. | UNINA-9910460461903321 |
Amsterdam : , : Elsevier, , 2015 | ||
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Lo trovi qui: Univ. Federico II | ||
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Plant cyclotides / / volume editor, David J. Craik, Institute for Molecular Bioscience, the University of Queensland, Brisbane, QLD, Australia |
Edizione | [First edition.] |
Pubbl/distr/stampa | Amsterdam : , : Elsevier, , 2015 |
Descrizione fisica | 1 online resource (404 p.) |
Collana | Advances in botanical research |
Soggetto topico |
Botany - Research
Plant molecular biology Plant proteomics Peptides Botanical chemistry |
ISBN |
0-12-800030-9
0-12-800797-4 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Front Cover; ADVANCES IN BOTANICAL RESEARCH; Plant Cyclotides; Copyright; Contents; CONTRIBUTORS; PREFACE; One - Overview on the Discovery and Applications of Cyclotides; 1. INTRODUCTION; ACKNOWLEDGMENTS; REFERENCES; Two - Cyclotides in the Violaceae; 1. THE DISCOVERY OF CYCLOTIDES IN VIOLACEAE; 2. UNLOCKING THE CYCLOTIDE LIBRARY; 3. THE VIOLACEAE; 4. VIOLACEAE-THE PHARMACOPOEIA; 5. GROWING NEEDS AND SOURCES OF CYCLOTIDES; 6. COMPLETING THE CIRCLE; ACKNOWLEDGMENTS; REFERENCES; Three - Cyclotides in the Rubiaceae; 1. INTRODUCTION; 2. DISCOVERY OF CYCLOTIDES
2.1 Cyclotide Analytical Screening Workflow2.2 Cyclotides Sequence Analysis Using Transcriptomics and Peptidomics; 3. DISTRIBUTION OF CYCLOTIDES IN RUBIACEAE; 3.1 Rubiaceae-An Overview; 3.2 Morphology and Taxonomy of Rubiaceae; 3.3 Distribution of Cyclotides within Rubiaceae; 3.4 Cyclotide Precursors of Rubiaceae Plants; 3.5 Cyclotide Sequence Variations within Rubiaceae; 3.6 Distribution of Cyclotides in Other Gentianales; 4. EVOLUTION OF CYCLOTIDES; 5. BIOACTIVITIES OF RUBIACEAE CYCLOTIDES; 6. CONCLUSION AND OUTLOOK; ACKNOWLEDGMENTS; REFERENCES; Four - Cyclotides from Chinese Plants 1. Introduction2. Chemical Detection Method for Cyclotides; 3. Distribution and Chemotaxonomy of Cyclotides in Chinese Plants; 4. Extraction, Isolation and Structural Elucidation of Cyclotides in Chinese Plants; 4.1 Extraction and Isolation of Cyclotides in Chinese Plants; 4.2 Tandem MS Sequencing of Cyclotides in Chinese Plants; 4.3 NMR Characterization of Cyclotides in Chinese Plants; 5. Biological Activity of Cyclotides in Chinese Plants; Acknowledgments; References; Five - Primary Structural Analysis of Cyclotides; 1. CYCLOTIDE DISCOVERY-UNTANGLING THE CYSTINE KNOT 2. TOOLS FOR PEPTIDE SEQUENCE ASSIGNMENT2.1 Gene Sequencing; 2.2 Genome Mining; 2.3 Next-Generation Sequencing; 2.4 Peptide Extraction and Purification; 2.5 Acid Hydrolysis and Amino Acid Analysis; 2.6 Edman Degradation; 2.7 Chemical and Enzymatic Digestion; 3. MASS SPECTROMETRY; 3.1 Ionization; 3.1.1 Electrospray Ionization; 3.1.2 Nanoelectrospray Ionization; 3.1.3 Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry; 3.2 Mass Analyzers; 3.2.1 Quadrupole Mass Analyzers; 3.2.2 TOF Mass Analyzers; 3.3 Peptide Sequencing; 4. APPLICATION OF MASS SPECTROMETRY TO CYCLOTIDE SEQUENCING 4.1 MS Analysis of Cyclotides4.2 Tandem Mass Spectrometric (MS/MS) Analysis of Cyclotides; 4.3 Application of "Omics" Technologies to Cyclotide Sequencing; 5. CHALLENGES AND COMPLEXITIES; 5.1 Co-eluting, Isobaric Peptides; 5.2 N/D Isoforms; 5.3 Unknown Genomes/Incomplete DBs; 6. FUTURE PROSPECTS; 6.1 Transcriptomics and Bioinformatics; 6.2 Automation and Robotics; 6.3 Advances in MS Hardware; 6.4 Advances in MS Software; 7. CONCLUDING REMARKS; REFERENCES; Six - Structural Studies of Cyclotides; 1. THE CYCLIC CYSTINE KNOT; 2. STRUCTURAL FEATURES OF CYCLOTIDES; 2.1 Structural Studies 2.2 Möbius, Bracelets, and Trypsin Inhibitors |
Record Nr. | UNINA-9910797819403321 |
Amsterdam : , : Elsevier, , 2015 | ||
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Lo trovi qui: Univ. Federico II | ||
|
Plant cyclotides / / volume editor, David J. Craik, Institute for Molecular Bioscience, the University of Queensland, Brisbane, QLD, Australia |
Edizione | [First edition.] |
Pubbl/distr/stampa | Amsterdam : , : Elsevier, , 2015 |
Descrizione fisica | 1 online resource (404 p.) |
Collana | Advances in botanical research |
Soggetto topico |
Botany - Research
Plant molecular biology Plant proteomics Peptides Botanical chemistry |
ISBN |
0-12-800030-9
0-12-800797-4 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Front Cover; ADVANCES IN BOTANICAL RESEARCH; Plant Cyclotides; Copyright; Contents; CONTRIBUTORS; PREFACE; One - Overview on the Discovery and Applications of Cyclotides; 1. INTRODUCTION; ACKNOWLEDGMENTS; REFERENCES; Two - Cyclotides in the Violaceae; 1. THE DISCOVERY OF CYCLOTIDES IN VIOLACEAE; 2. UNLOCKING THE CYCLOTIDE LIBRARY; 3. THE VIOLACEAE; 4. VIOLACEAE-THE PHARMACOPOEIA; 5. GROWING NEEDS AND SOURCES OF CYCLOTIDES; 6. COMPLETING THE CIRCLE; ACKNOWLEDGMENTS; REFERENCES; Three - Cyclotides in the Rubiaceae; 1. INTRODUCTION; 2. DISCOVERY OF CYCLOTIDES
2.1 Cyclotide Analytical Screening Workflow2.2 Cyclotides Sequence Analysis Using Transcriptomics and Peptidomics; 3. DISTRIBUTION OF CYCLOTIDES IN RUBIACEAE; 3.1 Rubiaceae-An Overview; 3.2 Morphology and Taxonomy of Rubiaceae; 3.3 Distribution of Cyclotides within Rubiaceae; 3.4 Cyclotide Precursors of Rubiaceae Plants; 3.5 Cyclotide Sequence Variations within Rubiaceae; 3.6 Distribution of Cyclotides in Other Gentianales; 4. EVOLUTION OF CYCLOTIDES; 5. BIOACTIVITIES OF RUBIACEAE CYCLOTIDES; 6. CONCLUSION AND OUTLOOK; ACKNOWLEDGMENTS; REFERENCES; Four - Cyclotides from Chinese Plants 1. Introduction2. Chemical Detection Method for Cyclotides; 3. Distribution and Chemotaxonomy of Cyclotides in Chinese Plants; 4. Extraction, Isolation and Structural Elucidation of Cyclotides in Chinese Plants; 4.1 Extraction and Isolation of Cyclotides in Chinese Plants; 4.2 Tandem MS Sequencing of Cyclotides in Chinese Plants; 4.3 NMR Characterization of Cyclotides in Chinese Plants; 5. Biological Activity of Cyclotides in Chinese Plants; Acknowledgments; References; Five - Primary Structural Analysis of Cyclotides; 1. CYCLOTIDE DISCOVERY-UNTANGLING THE CYSTINE KNOT 2. TOOLS FOR PEPTIDE SEQUENCE ASSIGNMENT2.1 Gene Sequencing; 2.2 Genome Mining; 2.3 Next-Generation Sequencing; 2.4 Peptide Extraction and Purification; 2.5 Acid Hydrolysis and Amino Acid Analysis; 2.6 Edman Degradation; 2.7 Chemical and Enzymatic Digestion; 3. MASS SPECTROMETRY; 3.1 Ionization; 3.1.1 Electrospray Ionization; 3.1.2 Nanoelectrospray Ionization; 3.1.3 Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry; 3.2 Mass Analyzers; 3.2.1 Quadrupole Mass Analyzers; 3.2.2 TOF Mass Analyzers; 3.3 Peptide Sequencing; 4. APPLICATION OF MASS SPECTROMETRY TO CYCLOTIDE SEQUENCING 4.1 MS Analysis of Cyclotides4.2 Tandem Mass Spectrometric (MS/MS) Analysis of Cyclotides; 4.3 Application of "Omics" Technologies to Cyclotide Sequencing; 5. CHALLENGES AND COMPLEXITIES; 5.1 Co-eluting, Isobaric Peptides; 5.2 N/D Isoforms; 5.3 Unknown Genomes/Incomplete DBs; 6. FUTURE PROSPECTS; 6.1 Transcriptomics and Bioinformatics; 6.2 Automation and Robotics; 6.3 Advances in MS Hardware; 6.4 Advances in MS Software; 7. CONCLUDING REMARKS; REFERENCES; Six - Structural Studies of Cyclotides; 1. THE CYCLIC CYSTINE KNOT; 2. STRUCTURAL FEATURES OF CYCLOTIDES; 2.1 Structural Studies 2.2 Möbius, Bracelets, and Trypsin Inhibitors |
Record Nr. | UNINA-9910818523503321 |
Amsterdam : , : Elsevier, , 2015 | ||
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Lo trovi qui: Univ. Federico II | ||
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Protection reactions, medicinal chemistry, combinatorial synthesis [[electronic resource] /] / edited by Andrew B. Hughes |
Edizione | [1st ed.] |
Pubbl/distr/stampa | Weinheim, Germany, : Wiley-VCH, 2011 |
Descrizione fisica | 1 online resource (553 p.) |
Disciplina | 547.7 |
Altri autori (Persone) | HughesAndrew B |
Collana | Amino acids, peptides and proteins in organic chemistry |
Soggetto topico |
Amino acids
Peptides Amino acids - Synthesis |
ISBN |
3-527-64157-2
1-283-14053-5 9786613140531 3-527-63183-6 3-527-63182-8 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | pt. 1. Amino acid-based peptidomimetics -- pt. 2. Medicinal chemistry of amino acids -- pt. 3. Amino acids in combinatorial synthesis. |
Record Nr. | UNINA-9910130852803321 |
Weinheim, Germany, : Wiley-VCH, 2011 | ||
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Lo trovi qui: Univ. Federico II | ||
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Protein and peptide folding, misfolding, and non-folding [[electronic resource] /] / edited by Reinhard Schweitzer-Stenner |
Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, c2012 |
Descrizione fisica | 1 online resource (596 p.) |
Disciplina | 572/.633 |
Altri autori (Persone) | Schweitzer-StennerReinhard |
Collana | Wiley series in protein and peptide science |
Soggetto topico |
Protein folding
Peptides |
ISBN |
1-280-59177-3
9786613621603 1-118-18335-5 1-118-18337-1 1-118-18334-7 |
Classificazione | SCI049000 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
PROTEIN AND PEPTIDE FOLDING, MISFOLDING, AND NON-FOLDING; CONTENTS; INTRODUCTION TO THE WILEY SERIES ON PROTEIN AND PEPTIDE SCIENCE; PREFACE; CONTRIBUTORS; INTRODUCTION; 1: WHY ARE WE INTERESTED IN THE UNFOLDED PEPTIDES AND PROTEINS? Vladimir N. Uversky and A. Keith Dunker; 1.1. INTRODUCTION; 1.2. WHY STUDY IDPS?; 1.3. LESSON 1: DISORDEREDNESS IS ENCODED IN THE AMINO ACID SEQUENCE AND CAN BE PREDICTED; 1.4. LESSON 2: DISORDERED PROTEINS ARE HIGHLY ABUNDANT IN NATURE; 1.5. LESSON 3: DISORDERED PROTEINS ARE GLOBALLY HETEROGENEOUS
1.6. LESSON 4: HYDRODYNAMIC DIMENSIONS OF NATIVELY UNFOLDED PROTEINS ARE CHARGE DEPENDENT1.7. LESSON 5: POLYMER PHYSICS EXPLAINS HYDRODYNAMIC BEHAVIOR OF DISORDERED PROTEINS; 1.8. LESSON 6: NATIVELY UNFOLDED PROTEINS ARE PLIABLE AND VERY SENSITIVE TO THEIR ENVIRONMENT; 1.9. LESSON 7: WHEN BOUND, NATIVELY UNFOLDED PROTEINS CAN GAIN UNUSUAL STRUCTURES; 1.10. LESSON 8: IDPS CAN FORM DISORDERED OR FUZZY COMPLEXES; 1.11. LESSON 9: INTRINSIC DISORDER IS CRUCIAL FOR RECOGNITION, REGULATION, AND SIGNALING; 1.12. LESSON 10: PROTEIN POSTTRANSLATIONAL MODIFICATIONS OCCUR AT DISORDERED REGIONS 1.13. LESSON 11: DISORDERED REGIONS ARE PRIMARY TARGETS FOR AS1.14. LESSON 12: DISORDERED PROTEINS ARE TIGHTLY REGULATED IN THE LIVING CELLS; 1.15. LESSON 13: NATIVELY UNFOLDED PROTEINS ARE FREQUENTLY ASSOCIATED WITH HUMAN DISEASES; 1.16. LESSON 14: NATIVELY UNFOLDED PROTEINS ARE ATTRACTIVE DRUG TARGETS; 1.17. LESSON 15: BRIGHT FUTURE OF FUZZY PROTEINS; ACKNOWLEDGMENTS; REFERENCES; I: CONFORMATIONAL ANALYSISOF UNFOLDED STATES; 2: EXPLORING THE ENERGY LANDSCAPE OF SMALL PEPTIDES AND PROTEINS BY MOLECULAR DYNAMICS SIMULATIONS Gerhard Stock, Abhinav Jain, Laura Riccardi, and Phuong H. Nguyen 2.1. INTRODUCTION: FREE ENERGY LANDSCAPES AND HOW TO CONSTRUCT THEM2.2. DIHEDRAL ANGLE PCA ALLOWS US TO SEPARATE INTERNAL AND GLOBAL MOTION; 2.3. DIMENSIONALITY OF THE FREE ENERGY LANDSCAPE; 2.4. CHARACTERIZATION OF THE FREE ENERGY LANDSCAPE: STATES, BARRIERS, AND TRANSITIONS; 2.5. LOW-DIMENSIONAL SIMULATION OF BIOMOLECULAR DYNAMICS TO CATCH SLOW AND RARE PROCESSES; 2.6. PCA BY PARTS: THE FOLDING PATHWAYS OF VILLIN HEADPIECE; 2.7. THE ENERGY LANDSCAPE OF AGGREGATING Aß-PEPTIDES; 2.8. CONCLUDING REMARKS; ACKNOWLEDGMENTS; REFERENCES 3: LOCAL BACKBONE PREFERENCES AND NEAREST-NEIGHBOR EFFECTS IN THE UNFOLDED AND NATIVE STATES Joe DeBartolo, Abhishek Jha, Karl F. Freed, and Tobin R. Sosnick3.1. INTRODUCTION; 3.2. EARLY DAYS: RANDOM COIL-THEORY AND EXPERIMENT; 3.3. DENATURED PROTEINS AS SELF-AVOIDING RANDOM COILS; 3.4. MODELING THE UNFOLDED STATE; 3.5. NN EFFECTS IN PROTEIN STRUCTURE PREDICTION; 3.6. UTILIZING FOLDING PATHWAYS FORSTRUCTURE PREDICTION; 3.7. NATIVE STATE MODELING; 3.8. SECONDARY-STRUCTURE PROPENSITIES: NATIVE BACKBONES IN UNFOLDED PROTEINS; 3.9. CONCLUSIONS; ACKNOWLEDGMENTS; REFERENCES 4: SHORT-DISTANCE FRET APPLIED TO THE POLYPEPTIDE CHAIN Maik H. Jacob and Werner M. Nau |
Record Nr. | UNINA-9910141317703321 |
Hoboken, N.J., : John Wiley & Sons, c2012 | ||
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Lo trovi qui: Univ. Federico II | ||
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Protein and peptide folding, misfolding, and non-folding [[electronic resource] /] / edited by Reinhard Schweitzer-Stenner |
Pubbl/distr/stampa | Hoboken, N.J., : John Wiley & Sons, c2012 |
Descrizione fisica | 1 online resource (596 p.) |
Disciplina | 572/.633 |
Altri autori (Persone) | Schweitzer-StennerReinhard |
Collana | Wiley series in protein and peptide science |
Soggetto topico |
Protein folding
Peptides |
ISBN |
1-280-59177-3
9786613621603 1-118-18335-5 1-118-18337-1 1-118-18334-7 |
Classificazione | SCI049000 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
PROTEIN AND PEPTIDE FOLDING, MISFOLDING, AND NON-FOLDING; CONTENTS; INTRODUCTION TO THE WILEY SERIES ON PROTEIN AND PEPTIDE SCIENCE; PREFACE; CONTRIBUTORS; INTRODUCTION; 1: WHY ARE WE INTERESTED IN THE UNFOLDED PEPTIDES AND PROTEINS? Vladimir N. Uversky and A. Keith Dunker; 1.1. INTRODUCTION; 1.2. WHY STUDY IDPS?; 1.3. LESSON 1: DISORDEREDNESS IS ENCODED IN THE AMINO ACID SEQUENCE AND CAN BE PREDICTED; 1.4. LESSON 2: DISORDERED PROTEINS ARE HIGHLY ABUNDANT IN NATURE; 1.5. LESSON 3: DISORDERED PROTEINS ARE GLOBALLY HETEROGENEOUS
1.6. LESSON 4: HYDRODYNAMIC DIMENSIONS OF NATIVELY UNFOLDED PROTEINS ARE CHARGE DEPENDENT1.7. LESSON 5: POLYMER PHYSICS EXPLAINS HYDRODYNAMIC BEHAVIOR OF DISORDERED PROTEINS; 1.8. LESSON 6: NATIVELY UNFOLDED PROTEINS ARE PLIABLE AND VERY SENSITIVE TO THEIR ENVIRONMENT; 1.9. LESSON 7: WHEN BOUND, NATIVELY UNFOLDED PROTEINS CAN GAIN UNUSUAL STRUCTURES; 1.10. LESSON 8: IDPS CAN FORM DISORDERED OR FUZZY COMPLEXES; 1.11. LESSON 9: INTRINSIC DISORDER IS CRUCIAL FOR RECOGNITION, REGULATION, AND SIGNALING; 1.12. LESSON 10: PROTEIN POSTTRANSLATIONAL MODIFICATIONS OCCUR AT DISORDERED REGIONS 1.13. LESSON 11: DISORDERED REGIONS ARE PRIMARY TARGETS FOR AS1.14. LESSON 12: DISORDERED PROTEINS ARE TIGHTLY REGULATED IN THE LIVING CELLS; 1.15. LESSON 13: NATIVELY UNFOLDED PROTEINS ARE FREQUENTLY ASSOCIATED WITH HUMAN DISEASES; 1.16. LESSON 14: NATIVELY UNFOLDED PROTEINS ARE ATTRACTIVE DRUG TARGETS; 1.17. LESSON 15: BRIGHT FUTURE OF FUZZY PROTEINS; ACKNOWLEDGMENTS; REFERENCES; I: CONFORMATIONAL ANALYSISOF UNFOLDED STATES; 2: EXPLORING THE ENERGY LANDSCAPE OF SMALL PEPTIDES AND PROTEINS BY MOLECULAR DYNAMICS SIMULATIONS Gerhard Stock, Abhinav Jain, Laura Riccardi, and Phuong H. Nguyen 2.1. INTRODUCTION: FREE ENERGY LANDSCAPES AND HOW TO CONSTRUCT THEM2.2. DIHEDRAL ANGLE PCA ALLOWS US TO SEPARATE INTERNAL AND GLOBAL MOTION; 2.3. DIMENSIONALITY OF THE FREE ENERGY LANDSCAPE; 2.4. CHARACTERIZATION OF THE FREE ENERGY LANDSCAPE: STATES, BARRIERS, AND TRANSITIONS; 2.5. LOW-DIMENSIONAL SIMULATION OF BIOMOLECULAR DYNAMICS TO CATCH SLOW AND RARE PROCESSES; 2.6. PCA BY PARTS: THE FOLDING PATHWAYS OF VILLIN HEADPIECE; 2.7. THE ENERGY LANDSCAPE OF AGGREGATING Aß-PEPTIDES; 2.8. CONCLUDING REMARKS; ACKNOWLEDGMENTS; REFERENCES 3: LOCAL BACKBONE PREFERENCES AND NEAREST-NEIGHBOR EFFECTS IN THE UNFOLDED AND NATIVE STATES Joe DeBartolo, Abhishek Jha, Karl F. Freed, and Tobin R. Sosnick3.1. INTRODUCTION; 3.2. EARLY DAYS: RANDOM COIL-THEORY AND EXPERIMENT; 3.3. DENATURED PROTEINS AS SELF-AVOIDING RANDOM COILS; 3.4. MODELING THE UNFOLDED STATE; 3.5. NN EFFECTS IN PROTEIN STRUCTURE PREDICTION; 3.6. UTILIZING FOLDING PATHWAYS FORSTRUCTURE PREDICTION; 3.7. NATIVE STATE MODELING; 3.8. SECONDARY-STRUCTURE PROPENSITIES: NATIVE BACKBONES IN UNFOLDED PROTEINS; 3.9. CONCLUSIONS; ACKNOWLEDGMENTS; REFERENCES 4: SHORT-DISTANCE FRET APPLIED TO THE POLYPEPTIDE CHAIN Maik H. Jacob and Werner M. Nau |
Record Nr. | UNINA-9910814089803321 |
Hoboken, N.J., : John Wiley & Sons, c2012 | ||
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Lo trovi qui: Univ. Federico II | ||
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Pseudo-peptides in drug discovery [[electronic resource] /] / [edited by] Peter E. Neilsen |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH, c2004 |
Descrizione fisica | 1 online resource (258 p.) |
Disciplina | 615.19 |
Altri autori (Persone) | NielsenPeter E. <1951-> |
Soggetto topico |
Peptide drugs - Design
Peptides Amino acids - Synthesis Polyamides |
Soggetto genere / forma | Electronic books. |
ISBN |
1-280-52069-8
9786610520695 3-527-60569-X 3-527-60190-2 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Pseudo-peptides in Drug Discovery; Contents; Preface; List of Contributors; 1 Versatile Oligo(N-Substituted) Glycines: The Many Roles of Peptoids in Drug Discovery; 1.1 Introduction; 1.2 Peptoid Synthesis; 1.2.1 Solid-Phase Synthesis; 1.2.2 Sub-monomer Solid-Phase Method; 1.2.3 Side Reactions; 1.2.4 Post-Synthetic Analysis; 1.3 Drug Discovery via Small-Molecule Peptoid Libraries; 1.3.1 Peptoid Drugs from Combinatorial Libraries; 1.3.2 Peptoid Inhibitors of RNA-Protein Interactions; 1.4 Peptoid-Based Drug Delivery and Molecular Transporters: Cellular Uptake
1.4.1 Peptoid Mimics of HIV-Tat Protein1.4.2 Cellular Delivery of Nucleic Acids; 1.5 Peptoid Mimics of Peptide Ligands; 1.6 Peptoids with Folded Structure; 1.6.1 Restricting Conformational Space; 1.6.2 Peptoid Helices; 1.6.2.1 CD and NMR Studies of a Helical Peptoid Pentamer with α-Chiral Aromatic Side Chains; 1.6.2.2 CD Studies of Longer Peptoid Helices Containing α-Chiral Aromatic Side Chains; 1.6.2.3 Structural Studies of Peptoids with Aliphatic Side Chains by CD, NMR, and X-ray Crystallography; 1.6.2.4 Summary; 1.6.3 Protein-mimetic Structures 1.7 Biomimetic Peptoid Structures for Therapeutic Applications1.7.1 Peptoid Mimics of Antibacterial Peptides; 1.7.2 Peptoid-Based Mimics of Lung Surfactant Proteins; 1.7.3 Collagen-based Structures Containing Peptoid Residues; 1.8 Obstacles to the Development of Biomedically-useful Peptoids; 1.8.1 Enhance the Diversity of Secondary Structure in Peptoid Foldamers; 1.8.2 Improve Understanding of Peptoid Sequence/Structure Relationships; 1.8.3 Translate Bioactive Peptide Sequences into Bioactive Peptoid Sequences; 1.8.4 Develop Peptoids with Stable Tertiary Structure 1.8.5 Develop Peptoid Shuttles for Intracellular Import of Xenobiotic Agents1.8.6 Optimize Pharmacological Profile of Oligopeptoids; 1.9 Conclusion; 1.10 References; 2 β-Peptides, γ-Peptides and Isosteric Backbones: New Scaffolds with Controlled Shapes for Mimicking Protein Secondary Structure Elements; 2.1 Introduction; 2.2 Molecular Organization in β-Peptide Oligomers; 2.2.1 Historical Background; 2.2.2 β-Amino Acids versus α-Amino Acids: An Enormous Increase in Chemical Diversity; 2.2.3 Helical Folds; 2.2.3.1 The 3(14)-Helix; 2.2.3.2 The 12/10- (10/12-) Helix; 2.2.3.3 The 2.5(12)-Helix 2.2.3.4 The 2(8)-Helix2.2.4 Extended β-Peptide Strands, Turns and Formation of Sheet Structures; 2.3 Molecular Organization in γ-Peptide Oligomers; 2.3.1 Preparation of γ-Amino Acid Monomers for γ-Peptide Synthesis; 2.3.2 Helical Folds; 2.3.3 Turn and Sheet Structures; 2.4 Biological Activities of β- and γ-Peptides; 2.4.1 Biological Stability; 2.4.2 Bioactive Peptides Based on Helical Scaffolds; 2.4.3 Bioactive Peptides Based on Open-Chain β-Turn Mimetics; 2.4.4 Cell Penetrating β-Peptides; 2.5 Isosteres; 2.5.1 Example 1: Oligomers of α-Aminooxy Acids as β-Peptide Mimetics 2.5.2 Example 2: N,N ́-Linked Oligoureas as γ-Peptide Mimetics |
Record Nr. | UNINA-9910146238203321 |
Weinheim, : Wiley-VCH, c2004 | ||
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Lo trovi qui: Univ. Federico II | ||
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